TY  - JOUR
A1  - Nichols, Parker J.
A1  - Born, Alexandra
A1  - Henen, Morkos A.
A1  - Strotz, Dean
A1  - Orts, Julien
A1  - Olsson, Simon
A1  - Güntert, Peter
A1  - Chi, Celestine N.
A1  - Vögeli, Beat
T1  - The exact nuclear Overhauser enhancement: recent advances
T2  - Molecules
N2  - Although often depicted as rigid structures, proteins are highly dynamic systems, whose motions are essential to their functions. Despite this, it is difficult to investigate protein dynamics due to the rapid timescale at which they sample their conformational space, leading most NMR-determined structures to represent only an averaged snapshot of the dynamic picture. While NMR relaxation measurements can help to determine local dynamics, it is difficult to detect translational or concerted motion, and only recently have significant advances been made to make it possible to acquire a more holistic representation of the dynamics and structural landscapes of proteins. Here, we briefly revisit our most recent progress in the theory and use of exact nuclear Overhauser enhancements (eNOEs) for the calculation of structural ensembles that describe their conformational space. New developments are primarily targeted at increasing the number and improving the quality of extracted eNOE distance restraints, such that the multi-state structure calculation can be applied to proteins of higher molecular weights. We then review the implications of the exact NOE to the protein dynamics and function of cyclophilin A and the WW domain of Pin1, and finally discuss our current research and future directions.
KW  - NMR
KW  - biological macromolecules
KW  - proteins
KW  - dynamics
KW  - correlated dynamics
KW  - exact NOE
KW  - structure calculation
KW  - structure ensemble
KW  - allostery
KW  - conformational space
Y1  - 2017
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/44711
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-447114
N1  - This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
VL  - 22
IS  - 1176
ER  -